MolNFT v1 · #177292 · protein + DNA
Human P53 core domain with germline hot spot mutation M133T in complex with the natural PIG3 P53-response element and arsenic
7EDS · Cellular tumor antigen P53: “Human P53 core domain with germline hot spot mutation M133T in complex with the natural PIG3 P53-response…”. X-ray diffraction, 2 ligands (ARS, ZN), 3 pockets (best druggability 0.62). MolNFT v1 #177292…
- PDB
- 7EDS
- Type
- protein + DNA
- Length
- 253 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular tumor antigen P53; PIG3 sense strand; PIG3 anti-sense strand
- UniProt
- P04637
- Ligands
- ARS, ZN
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 3 distinct chains · 12% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellular tumor antigen P53 | protein | 193 | 12% helix, 35% strand | P04637 |
| R | PIG3 sense strand | dna | 30 | — | — |
| F | PIG3 anti-sense strand | dna | 30 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.62 | 0.76 | 43 | empty |
| 2 | 184 | 0.43 | 0.73 | 17 | empty |
| 3 | 88 | 0.36 | 0.75 | 21 | empty |
Interfaces
3 interfaces between chains.
- R–F · 1407 Ų buried · 168 hydrogen bonds · nucleic-nucleic
- A–R · 314 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–F · 111 Ų buried · 2 hydrogen bonds · protein-nucleic
Compared structures
- 7EDS · Human p53 core domain with germline hot spot mutation M133T in complex with the natural… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 7EDS · PDBe 7EDS · UniProt P04637
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.